메뉴 건너뛰기




Volumn 17, Issue C, 1996, Pages 127-148

Translocation of Preproteins Across the Mitochondrial Inner Membrane: Tims and HSP70

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0000201147     PISSN: 15692558     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1569-2558(09)60012-6     Document Type: Article
Times cited : (3)

References (83)
  • 2
    • 0025597095 scopus 로고
    • A yeast mitochondrial outer membrane protein essential for protein import and cell viability
    • Baker K.P., Schaniel A., Vestweber D., and Schatz G. A yeast mitochondrial outer membrane protein essential for protein import and cell viability. Nature 348 (1990) 605-609
    • (1990) Nature , vol.348 , pp. 605-609
    • Baker, K.P.1    Schaniel, A.2    Vestweber, D.3    Schatz, G.4
  • 3
    • 0029070886 scopus 로고
    • The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system
    • Berthold J., Bauer M.F., Schneider H.-C., Klaus C., Dietmeier K., Neupert W., and Brunner M. The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system. Cell 81 (1995) 1085-1093
    • (1995) Cell , vol.81 , pp. 1085-1093
    • Berthold, J.1    Bauer, M.F.2    Schneider, H.-C.3    Klaus, C.4    Dietmeier, K.5    Neupert, W.6    Brunner, M.7
  • 4
    • 0029094657 scopus 로고
    • Functional and physical interactions of components of the yeast mitochondrial inner membrane import machinery (MIM)
    • Blom J., Dekker P.J.T., and Meijer M. Functional and physical interactions of components of the yeast mitochondrial inner membrane import machinery (MIM). Eur. J. Biochem. 232 (1995) 309-314
    • (1995) Eur. J. Biochem. , vol.232 , pp. 309-314
    • Blom, J.1    Dekker, P.J.T.2    Meijer, M.3
  • 5
    • 0027360995 scopus 로고
    • The essential yeast protein MIM44 (encoded by MP***11) is involved in an early step of preprotein translocation across the mitochondrial inner membrane
    • Blom J., Kübrich M., Rassow J., Voos W., Dekker P.J.T., Maarse A.C., Meijer M., and Pfanner N. The essential yeast protein MIM44 (encoded by MP***11) is involved in an early step of preprotein translocation across the mitochondrial inner membrane. Mol. Cell. Biol. 13 (1993) 7364-7371
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7364-7371
    • Blom, J.1    Kübrich, M.2    Rassow, J.3    Voos, W.4    Dekker, P.J.T.5    Maarse, A.C.6    Meijer, M.7    Pfanner, N.8
  • 6
    • 0023644921 scopus 로고
    • Phosphodiester bond cleavage outside mitochondria is required for the completion of protein import into the mitochondrial matrix
    • Chen W.-J., and Douglas M.G. Phosphodiester bond cleavage outside mitochondria is required for the completion of protein import into the mitochondrial matrix. Cell 49 (1987) 651-658
    • (1987) Cell , vol.49 , pp. 651-658
    • Chen, W.-J.1    Douglas, M.G.2
  • 8
    • 0027300506 scopus 로고
    • Heat shock proteins: Molecular chaperones of protein biogenesis
    • Craig E.A., Gambill B.D., and Nelson R.J. Heat shock proteins: Molecular chaperones of protein biogenesis. Microbiol. Rev. 57 (1993) 402-414
    • (1993) Microbiol. Rev. , vol.57 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 10
    • 0027515288 scopus 로고
    • A matrix ATP requirement for presequence translocation across the inner membrane of mitochondria
    • Cyr D.M., Stuart R.A., and Neupert W. A matrix ATP requirement for presequence translocation across the inner membrane of mitochondria. J. Biol. Chem. 268 (1993) 23751-23754
    • (1993) J. Biol. Chem. , vol.268 , pp. 23751-23754
    • Cyr, D.M.1    Stuart, R.A.2    Neupert, W.3
  • 11
    • 0027222059 scopus 로고
    • Identification of MIM23, a putative component of the protein import machinery of the mitochondrial inner membrane
    • Dekker P.J.T., Keil P., Rassow J., Maarse A.C., Pfanner N., and Meijer M. Identification of MIM23, a putative component of the protein import machinery of the mitochondrial inner membrane. FEBS Lett. 330 (1993) 66-70
    • (1993) FEBS Lett. , vol.330 , pp. 66-70
    • Dekker, P.J.T.1    Keil, P.2    Rassow, J.3    Maarse, A.C.4    Pfanner, N.5    Meijer, M.6
  • 12
    • 0025968923 scopus 로고
    • Proton transfer is rate-limiting for translocation of precursor proteins by the Escherichia coll translocase
    • Driessen A.J.M., and Wickner W. Proton transfer is rate-limiting for translocation of precursor proteins by the Escherichia coll translocase. Proc. Natl. Acad. Sci. USA 88 (1991) 2471-2475
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2471-2475
    • Driessen, A.J.M.1    Wickner, W.2
  • 13
    • 0027162057 scopus 로고
    • MAS6 encodes an essential inner membrane component of the yeast mitochondrial protein import pathway
    • Emtage J.L.T., and Jensen R.E. MAS6 encodes an essential inner membrane component of the yeast mitochondrial protein import pathway. J. Cell Biol. 122 (1993) 1003-1012
    • (1993) J. Cell Biol. , vol.122 , pp. 1003-1012
    • Emtage, J.L.T.1    Jensen, R.E.2
  • 14
    • 0027490849 scopus 로고
    • A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins
    • Gambill D., Voos W., Kang P.J., Miao B., Langer T., Craig E.A., and Pfanner N. A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins. J. Cell Biol. 123 (1993) 109-117
    • (1993) J. Cell Biol. , vol.123 , pp. 109-117
    • Gambill, D.1    Voos, W.2    Kang, P.J.3    Miao, B.4    Langer, T.5    Craig, E.A.6    Pfanner, N.7
  • 15
    • 0028963263 scopus 로고
    • Mitochondrial import of COXVa characterized with yeast mutants: independence from receptors, but requirement for matrix hsp70 translocase function
    • Gärtner F., Voos W., Querol A., Miller B., Craig E.A., Cumsky M.G., and Pfanner N. Mitochondrial import of COXVa characterized with yeast mutants: independence from receptors, but requirement for matrix hsp70 translocase function. J. Biol. Chem. 270 (1995) 3788-3795
    • (1995) J. Biol. Chem. , vol.270 , pp. 3788-3795
    • Gärtner, F.1    Voos, W.2    Querol, A.3    Miller, B.4    Craig, E.A.5    Cumsky, M.G.6    Pfanner, N.7
  • 16
    • 0028834046 scopus 로고
    • Can hsp70 proteins act as force-generating motors?
    • Glick B.S. Can hsp70 proteins act as force-generating motors?. Cell 80 (1995) 11-14
    • (1995) Cell , vol.80 , pp. 11-14
    • Glick, B.S.1
  • 17
    • 0027332553 scopus 로고
    • 2 to the mitochondrial intermembrane space: The tightly folded heme-binding domain makes import dependent upon matrix ATP
    • 2 to the mitochondrial intermembrane space: The tightly folded heme-binding domain makes import dependent upon matrix ATP. Protein Science 2 (1993) 1901-1917
    • (1993) Protein Science , vol.2 , pp. 1901-1917
    • Glick, B.S.1    Wachter, C.2    Reid, G.A.3    Schatz, G.4
  • 18
    • 0027418577 scopus 로고
    • A mitochondrial import factor purified from rat liver cytosol is an ATP-dependent conformational modulator for precursor proteins
    • Hachiya N., Alam R., Sakasegawa Y., Sakaguchi M., Mihara K., and Omura T. A mitochondrial import factor purified from rat liver cytosol is an ATP-dependent conformational modulator for precursor proteins. EMBO J. 12 (1993) 1579-1586
    • (1993) EMBO J. , vol.12 , pp. 1579-1586
    • Hachiya, N.1    Alam, R.2    Sakasegawa, Y.3    Sakaguchi, M.4    Mihara, K.5    Omura, T.6
  • 21
    • 0029875083 scopus 로고    scopus 로고
    • The mitochondrial import motor: Dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis
    • Horst M., Oppliger W., Feifel B., Schatz G., and Glick B.S. The mitochondrial import motor: Dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis. Protein Science 5 (1996) 759-767
    • (1996) Protein Science , vol.5 , pp. 759-767
    • Horst, M.1    Oppliger, W.2    Feifel, B.3    Schatz, G.4    Glick, B.S.5
  • 23
    • 0024853819 scopus 로고
    • Translocation of proteins across the mitochondrial inner membrane, but not into the outer membrane, requires nucleoside triphosphates in the matrix
    • Hwang S.T., and Schatz G. Translocation of proteins across the mitochondrial inner membrane, but not into the outer membrane, requires nucleoside triphosphates in the matrix. Proc. Natl. Acad. Sci. USA 86 (1989) 8432-8436
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8432-8436
    • Hwang, S.T.1    Schatz, G.2
  • 24
    • 0024327616 scopus 로고
    • Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane
    • Hwang S., Jascur T., Vestweber D., Pon L., and Schatz G. Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane. J. Cell Biol. 109 (1989) 487-493
    • (1989) J. Cell Biol. , vol.109 , pp. 487-493
    • Hwang, S.1    Jascur, T.2    Vestweber, D.3    Pon, L.4    Schatz, G.5
  • 25
    • 0025833743 scopus 로고
    • Protein import into the yeast mitochondrial matrix: a new translocation intermediate between the two mitochondrial membranes
    • Hwang S.T., Wachter C., and Schatz G. Protein import into the yeast mitochondrial matrix: a new translocation intermediate between the two mitochondrial membranes. J. Biol. Chem. 266 (1991) 21083-21089
    • (1991) J. Biol. Chem. , vol.266 , pp. 21083-21089
    • Hwang, S.T.1    Wachter, C.2    Schatz, G.3
  • 26
    • 0024199388 scopus 로고
    • Import of proteins into yeast mitochondria: The nuclear MAS2 gene encodes a component of the processing protease that is homologous to the MASI-encoded subunit
    • Jensen R.E., and Yaffe M.P. Import of proteins into yeast mitochondria: The nuclear MAS2 gene encodes a component of the processing protease that is homologous to the MASI-encoded subunit. EMBO J. 7 (1988) 3863-3871
    • (1988) EMBO J. , vol.7 , pp. 3863-3871
    • Jensen, R.E.1    Yaffe, M.P.2
  • 27
    • 0025039149 scopus 로고
    • Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • Kang P.J., Ostermann J., Shilling J., Neupert W., Craig E.A., and Pfanner N. Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature 348 (1990) 137-143
    • (1990) Nature , vol.348 , pp. 137-143
    • Kang, P.J.1    Ostermann, J.2    Shilling, J.3    Neupert, W.4    Craig, E.A.5    Pfanner, N.6
  • 28
    • 0016613097 scopus 로고
    • Cytoplasmic type 80S ribosomes associated with yeast mitochondria. IV. Attachment of ribosomes to the outer membrane of isolated mitochondria
    • Kellems R.E., Allison V.F., and Butow R.A. Cytoplasmic type 80S ribosomes associated with yeast mitochondria. IV. Attachment of ribosomes to the outer membrane of isolated mitochondria. J. Cell Biol. 65 (1975) 1-14
    • (1975) J. Cell Biol. , vol.65 , pp. 1-14
    • Kellems, R.E.1    Allison, V.F.2    Butow, R.A.3
  • 29
    • 0024558293 scopus 로고
    • Molecular aspects of isolated and reconstituted carrier proteins from animal mitochondria
    • Kramer R., and Palmieri F. Molecular aspects of isolated and reconstituted carrier proteins from animal mitochondria. Biochim. Biophys. Acta 974 (1989) 1-23
    • (1989) Biochim. Biophys. Acta , vol.974 , pp. 1-23
    • Kramer, R.1    Palmieri, F.2
  • 30
    • 0028556615 scopus 로고
    • Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane
    • Kronidou N.G., Oppliger W., Bolliger L., Hannavy K., Glick B.S., Schatz G., and Horst M. Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane. Proc. Natl. Acad. Sci. USA 91 (1994) 12818-12822
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12818-12822
    • Kronidou, N.G.1    Oppliger, W.2    Bolliger, L.3    Hannavy, K.4    Glick, B.S.5    Schatz, G.6    Horst, M.7
  • 31
    • 0028142495 scopus 로고
    • The polytopic mitochondrial inner membrane proteins MIM17 and MIM23 operate at the same preprotein import site
    • Kübrich M., Keil P., Rassow J., Dekker P.J.T., Blom J., Meijer M., and Pfanner N. The polytopic mitochondrial inner membrane proteins MIM17 and MIM23 operate at the same preprotein import site. FEBS Lett. 349 (1994) 222-228
    • (1994) FEBS Lett. , vol.349 , pp. 222-228
    • Kübrich, M.1    Keil, P.2    Rassow, J.3    Dekker, P.J.T.4    Blom, J.5    Meijer, M.6    Pfanner, N.7
  • 32
    • 0028356858 scopus 로고
    • A role for a eukaryotic grpE-related protein, Mge 1p, in protein translocation
    • Laloraya S., Gambill B.D., and Craig E.A. A role for a eukaryotic grpE-related protein, Mge 1p, in protein translocation. Proc. Natl. Acad. Sci. USA 91 (1994) 6481-6485
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6481-6485
    • Laloraya, S.1    Gambill, B.D.2    Craig, E.A.3
  • 33
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer T., Lu C., Echols H., Flanagan J., Hayer M.K., and Hartl F.-U. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356 (1992) 683-689
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.-U.6
  • 34
    • 0028046512 scopus 로고
    • The mitochondrial outer membrane protein Mas22p is essential for protein import and viability of yeast
    • Lithgow T., Junne T., Suda K., Gratzer S., and Schatz G. The mitochondrial outer membrane protein Mas22p is essential for protein import and viability of yeast. Proc. Natl. Acad. Sci. USA 91 (1994) 11973-11977
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11973-11977
    • Lithgow, T.1    Junne, T.2    Suda, K.3    Gratzer, S.4    Schatz, G.5
  • 35
    • 0026657841 scopus 로고
    • MP***II, an essential gene encoding a mitochondrial membrane protein, is possibly involved in protein import into yeast mitochondria
    • Maarse A.C., Blom J., Grivell L.A., and Meijer M. MP***II, an essential gene encoding a mitochondrial membrane protein, is possibly involved in protein import into yeast mitochondria. EMBO J. 11 (1992) 3619-3628
    • (1992) EMBO J. , vol.11 , pp. 3619-3628
    • Maarse, A.C.1    Blom, J.2    Grivell, L.A.3    Meijer, M.4
  • 36
    • 0027934739 scopus 로고
    • Identification of the essential yeast protein MIM17, an integral mitochondrial inner membrane protein involved in protein import
    • Maarse A.C., Blom J., Keil P., Pfanner N., and Meijer M. Identification of the essential yeast protein MIM17, an integral mitochondrial inner membrane protein involved in protein import. FEBS Lett. 349 (1994) 215-221
    • (1994) FEBS Lett. , vol.349 , pp. 215-221
    • Maarse, A.C.1    Blom, J.2    Keil, P.3    Pfanner, N.4    Meijer, M.5
  • 37
    • 0027287709 scopus 로고
    • Import of a mitochondrial presequence into protein-free phospholipid vesicles
    • Maduke M., and Roise D. Import of a mitochondrial presequence into protein-free phospholipid vesicles. Science 260 (1993) 364-367
    • (1993) Science , vol.260 , pp. 364-367
    • Maduke, M.1    Roise, D.2
  • 38
    • 0026070260 scopus 로고
    • Sequential action of mitochondrial chaperones in protein import into the matrix
    • Manning-Krieg U.C., Scherer P.E., and Schatz G. Sequential action of mitochondrial chaperones in protein import into the matrix. EMBO J. 10 (1991) 3273-3280
    • (1991) EMBO J. , vol.10 , pp. 3273-3280
    • Manning-Krieg, U.C.1    Scherer, P.E.2    Schatz, G.3
  • 39
    • 0025953614 scopus 로고
    • Role of an energized inner membrane in mitochondrial protein import: δ drives the movement of presequences
    • Martin J., Mahlke K., and Pfanner N. Role of an energized inner membrane in mitochondrial protein import: δ drives the movement of presequences. J. Biol. Chem. 266 (1991) 18051-18057
    • (1991) J. Biol. Chem. , vol.266 , pp. 18051-18057
    • Martin, J.1    Mahlke, K.2    Pfanner, N.3
  • 40
    • 0024268186 scopus 로고
    • 70-kD heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria
    • Murakami H., Pain D., and Blobel G. 70-kD heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria. J. Cell Biol. 107 (1988) 2051-2057
    • (1988) J. Cell Biol. , vol.107 , pp. 2051-2057
    • Murakami, H.1    Pain, D.2    Blobel, G.3
  • 42
    • 0023377040 scopus 로고
    • Disruption of the outer membrane restores protein import to trypsintreated yeast mitochondria
    • Ohba M., and Schatz G. Disruption of the outer membrane restores protein import to trypsintreated yeast mitochondria. EMBO J. 6 (1987) 2117-2122
    • (1987) EMBO J. , vol.6 , pp. 2117-2122
    • Ohba, M.1    Schatz, G.2
  • 43
    • 0024458504 scopus 로고
    • Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
    • Ostermann J., Horwich A.L., Neupert W., and Hartl F.-U. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature 341 (1989) 125-130
    • (1989) Nature , vol.341 , pp. 125-130
    • Ostermann, J.1    Horwich, A.L.2    Neupert, W.3    Hartl, F.-U.4
  • 44
    • 0025667283 scopus 로고
    • Precursor proteins in transit through mitochondrial contact sites interact with hsp70 in the matrix
    • Ostermann J., Voos W., Kang P.J., Craig E.A., Neupert W., and Pfanner N. Precursor proteins in transit through mitochondrial contact sites interact with hsp70 in the matrix. FEBS Lett. 277 (1990) 281-284
    • (1990) FEBS Lett. , vol.277 , pp. 281-284
    • Ostermann, J.1    Voos, W.2    Kang, P.J.3    Craig, E.A.4    Neupert, W.5    Pfanner, N.6
  • 45
    • 0029240213 scopus 로고
    • Protein sorting: Pulling in the proteins
    • Pfanner N., and Meijer M. Protein sorting: Pulling in the proteins. Curr. Biol. 5 (1995) 132-135
    • (1995) Curr. Biol. , vol.5 , pp. 132-135
    • Pfanner, N.1    Meijer, M.2
  • 46
    • 0022159364 scopus 로고
    • Transport of proteins into mitochondria: A potassium diffusion potential is able to drive the import of ADP/ATP carrier
    • Pfanner N., and Neupert W. Transport of proteins into mitochondria: A potassium diffusion potential is able to drive the import of ADP/ATP carrier. EMBO J. 4 (1985) 2819-2825
    • (1985) EMBO J. , vol.4 , pp. 2819-2825
    • Pfanner, N.1    Neupert, W.2
  • 47
    • 0023644933 scopus 로고
    • Distinct steps in the import of ADP/ATP carrier into mitochondria
    • Pfanner N., and Neupert W. Distinct steps in the import of ADP/ATP carrier into mitochondria. J. Biol. Chem. 262 (1987) 7528-7536
    • (1987) J. Biol. Chem. , vol.262 , pp. 7528-7536
    • Pfanner, N.1    Neupert, W.2
  • 49
    • 0023645869 scopus 로고
    • The carboxyl-terminal two-thirds of the ADP/ATP carrier polypeptide contains sufficient information to direct translocation into mitochondria
    • Pfanner N., Hoeben P., Tropschug M., and Neupert W. The carboxyl-terminal two-thirds of the ADP/ATP carrier polypeptide contains sufficient information to direct translocation into mitochondria. J. Biol. Chem. 262 (1987) 14851-14854
    • (1987) J. Biol. Chem. , vol.262 , pp. 14851-14854
    • Pfanner, N.1    Hoeben, P.2    Tropschug, M.3    Neupert, W.4
  • 50
    • 0023659499 scopus 로고
    • Mitochondrial protein import: nucleoside triphosphates are involved in conferring import-competence to precursors
    • Pfanner N., Tropschug M., and Neupert W. Mitochondrial protein import: nucleoside triphosphates are involved in conferring import-competence to precursors. Cell 49 (1987) 815-823
    • (1987) Cell , vol.49 , pp. 815-823
    • Pfanner, N.1    Tropschug, M.2    Neupert, W.3
  • 51
    • 0023920952 scopus 로고
    • Role of ATP in mitochondrial protein import: Conformational alteration of a precursor protein can substitute for ATP requirement
    • Pfanner N., Pfaller R., Kleene R., Ito M., Tropschug M., and Neupert W. Role of ATP in mitochondrial protein import: Conformational alteration of a precursor protein can substitute for ATP requirement. J. Biol. Chem. 263 (1988) 4049-4051
    • (1988) J. Biol. Chem. , vol.263 , pp. 4049-4051
    • Pfanner, N.1    Pfaller, R.2    Kleene, R.3    Ito, M.4    Tropschug, M.5    Neupert, W.6
  • 52
    • 0025008104 scopus 로고
    • Energy requirements for unfolding and membrane translocation of precursor proteins during import into mitochondria
    • Pfanner N., Rassow J., Guiard B., Sollner T., Hartl F.-U., and Neupert W. Energy requirements for unfolding and membrane translocation of precursor proteins during import into mitochondria. J. Biol. Chem. 265 (1990) 16324-16329
    • (1990) J. Biol. Chem. , vol.265 , pp. 16324-16329
    • Pfanner, N.1    Rassow, J.2    Guiard, B.3    Sollner, T.4    Hartl, F.-U.5    Neupert, W.6
  • 53
    • 0026553323 scopus 로고
    • A dynamic model of the mitochondrial protein import machinery
    • Pfanner N., Rassow J., van der Klei I.J., and Neupert W. A dynamic model of the mitochondrial protein import machinery. Cell 68 (1992) 999-1002
    • (1992) Cell , vol.68 , pp. 999-1002
    • Pfanner, N.1    Rassow, J.2    van der Klei, I.J.3    Neupert, W.4
  • 54
    • 0027963264 scopus 로고
    • The protein import machinery of the mitochondrial inner membrane
    • Pfanner N., Craig E.A., and Meijer M. The protein import machinery of the mitochondrial inner membrane. Trends Biochem. Sci. 19 (1994) 368-372
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 368-372
    • Pfanner, N.1    Craig, E.A.2    Meijer, M.3
  • 55
    • 0024119655 scopus 로고
    • The processing peptidase of yeast mitochondria: The two cooperating components MPP and PEP are structurally related
    • Pollock R.A., Hartl F.-U., Cheng M.Y., Ostermann J., Horwich A., and Neupert W. The processing peptidase of yeast mitochondria: The two cooperating components MPP and PEP are structurally related. EMBO J. 7 (1988) 3493-3500
    • (1988) EMBO J. , vol.7 , pp. 3493-3500
    • Pollock, R.A.1    Hartl, F.-U.2    Cheng, M.Y.3    Ostermann, J.4    Horwich, A.5    Neupert, W.6
  • 56
    • 0026471714 scopus 로고
    • Transport of proteins across the endoplasmic reticulum membrane
    • Rapoport T.A. Transport of proteins across the endoplasmic reticulum membrane. Science 258 (1992) 931-936
    • (1992) Science , vol.258 , pp. 931-936
    • Rapoport, T.A.1
  • 57
    • 0026040249 scopus 로고
    • Mitochondrial preproteins en route from the outer membrane to the inner membrane are exposed to the intermembrane space
    • Rassow J., and Pfanner N. Mitochondrial preproteins en route from the outer membrane to the inner membrane are exposed to the intermembrane space. FEBS Lett. 293 (1991) 85-88
    • (1991) FEBS Lett. , vol.293 , pp. 85-88
    • Rassow, J.1    Pfanner, N.2
  • 59
    • 0024456399 scopus 로고
    • Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
    • Rothman J.E. Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells. Cell 59 (1989) 591-601
    • (1989) Cell , vol.59 , pp. 591-601
    • Rothman, J.E.1
  • 60
    • 0028284879 scopus 로고
    • Mdj 1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding
    • Rowley N., Prip-Buus C., Westermann B., Brown C., Schwarz E., Barrell B., and Neupert W. Mdj 1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77 (1994) 249-259
    • (1994) Cell , vol.77 , pp. 249-259
    • Rowley, N.1    Prip-Buus, C.2    Westermann, B.3    Brown, C.4    Schwarz, E.5    Barrell, B.6    Neupert, W.7
  • 61
    • 0027368167 scopus 로고
    • Masóp can be cross-linked to an arrested precursor and interacts with other proteins during mitochondrial protein import
    • Ryan K.R., and Jensen R.E. Masóp can be cross-linked to an arrested precursor and interacts with other proteins during mitochondrial protein import. J. Biol. Chem. 268 (1993) 23743-23746
    • (1993) J. Biol. Chem. , vol.268 , pp. 23743-23746
    • Ryan, K.R.1    Jensen, R.E.2
  • 62
    • 0028337259 scopus 로고
    • SMS1, a high-copy suppressor of the yeast masö mutant, encodes an essential inner membrane protein required for mitochondrial protein import
    • Ryan K.R., Menold M.M., Garrett S., and Jensen R.E. SMS1, a high-copy suppressor of the yeast masö mutant, encodes an essential inner membrane protein required for mitochondrial protein import. Mol. Biol. Cell 5 (1994) 529-538
    • (1994) Mol. Biol. Cell , vol.5 , pp. 529-538
    • Ryan, K.R.1    Menold, M.M.2    Garrett, S.3    Jensen, R.E.4
  • 63
    • 0026766661 scopus 로고
    • Polypeptide translocation across the endoplasmic reticulum membrane
    • Sanders S.L., and Schekman R. Polypeptide translocation across the endoplasmic reticulum membrane. J. Biol. Chem. 267 (1992) 13791-13794
    • (1992) J. Biol. Chem. , vol.267 , pp. 13791-13794
    • Sanders, S.L.1    Schekman, R.2
  • 64
    • 0027049693 scopus 로고
    • Identification of a 45-kDa protein at the protein import site of the yeast mitochondrial inner membrane
    • Scherer P.E., Manning-Krieg U.C., Jenö P., Schatz G., and Horst M. Identification of a 45-kDa protein at the protein import site of the yeast mitochondrial inner membrane. Proc. Natl. Acad. Sci. USA 89 (1992) 11930-11934
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11930-11934
    • Scherer, P.E.1    Manning-Krieg, U.C.2    Jenö, P.3    Schatz, G.4    Horst, M.5
  • 65
    • 0026073817 scopus 로고
    • + and ATP function at different steps of the catalytic cycle of preprotein translocase
    • + and ATP function at different steps of the catalytic cycle of preprotein translocase. Cell 64 (1991) 927-939
    • (1991) Cell , vol.64 , pp. 927-939
    • Schiebel, E.1    Driessen, A.J.M.2    Hartl, F.-U.3    Wickner, W.4
  • 66
    • 0022404366 scopus 로고
    • Transport of proteins into mitochondria: Translocational intermediates spanning contact sites between outer and inner membranes
    • Schleyer M., and Neupert W. Transport of proteins into mitochondria: Translocational intermediates spanning contact sites between outer and inner membranes. Cell 43 (1985) 339-350
    • (1985) Cell , vol.43 , pp. 339-350
    • Schleyer, M.1    Neupert, W.2
  • 67
    • 0021753883 scopus 로고
    • Processing peptidase of Neurospora mitochondria: Two-step cleavage of imported ATPase subunit 9
    • Schmidt B., Wachter E., Sebald W., and Neupert W. Processing peptidase of Neurospora mitochondria: Two-step cleavage of imported ATPase subunit 9. Eur. J. Biochem. 144 (1984) 581-588
    • (1984) Eur. J. Biochem. , vol.144 , pp. 581-588
    • Schmidt, B.1    Wachter, E.2    Sebald, W.3    Neupert, W.4
  • 70
    • 0023992840 scopus 로고
    • ADP-ATP carrier of Saccharomyces cerevisiae contains a mitochondrial import signal between amino acids 72 and 111
    • Smagula C.S., and Douglas M.G. ADP-ATP carrier of Saccharomyces cerevisiae contains a mitochondrial import signal between amino acids 72 and 111. J. Cell. Biochem. 36 (1988) 323-328
    • (1988) J. Cell. Biochem. , vol.36 , pp. 323-328
    • Smagula, C.S.1    Douglas, M.G.2
  • 71
    • 84989694486 scopus 로고
    • The protein import apparatus of chloroplasts
    • Soil J., and Alefsen H. The protein import apparatus of chloroplasts. Physiol. Plant. 87 (1993) 433-440
    • (1993) Physiol. Plant. , vol.87 , pp. 433-440
    • Soil, J.1    Alefsen, H.2
  • 72
    • 0025931801 scopus 로고
    • Analysis of mitochondrial protein import using translocation intermediates and specific antibodies
    • Sollner T., Rassow J., and Pfanner N. Analysis of mitochondrial protein import using translocation intermediates and specific antibodies. Meth. Cell Biol. 34 (1991) 345-358
    • (1991) Meth. Cell Biol. , vol.34 , pp. 345-358
    • Sollner, T.1    Rassow, J.2    Pfanner, N.3
  • 73
    • 13144251232 scopus 로고
    • Mitochondrial molecular chaperones: Their role in protein translocation
    • Stuart R.A., Cyr D.M., Craig E.A., and Neupert W. Mitochondrial molecular chaperones: Their role in protein translocation. Trends Biochem. Sci. 19 (1994) 87-92
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 87-92
    • Stuart, R.A.1    Cyr, D.M.2    Craig, E.A.3    Neupert, W.4
  • 74
    • 0029670827 scopus 로고    scopus 로고
    • The δ and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria
    • Ungermann C., Guiard B., Neupert W., and Cyrr D.M. The δ and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria. EMBO J. 15 (1996) 735-744
    • (1996) EMBO J. , vol.15 , pp. 735-744
    • Ungermann, C.1    Guiard, B.2    Neupert, W.3    Cyrr, D.M.4
  • 75
    • 0028117097 scopus 로고
    • The role of hsp70 in conferring unidirectionality on protein translocation into mitochondria
    • Ungermann C., Neupert W., and Cyr D.M. The role of hsp70 in conferring unidirectionality on protein translocation into mitochondria. Science 266 (1994) 1250-1253
    • (1994) Science , vol.266 , pp. 1250-1253
    • Ungermann, C.1    Neupert, W.2    Cyr, D.M.3
  • 76
    • 0343040690 scopus 로고
    • Import of an incompletely folded precursor protein into isolated mitochondria requires an energized inner membrane, but no added ATP
    • Verner K., and Schatz G. Import of an incompletely folded precursor protein into isolated mitochondria requires an energized inner membrane, but no added ATP. EMBO J. 6 (1987) 2449-2456
    • (1987) EMBO J. , vol.6 , pp. 2449-2456
    • Verner, K.1    Schatz, G.2
  • 77
    • 0024202929 scopus 로고
    • A chimeric mitochondrial precursor protein with internal disulfide bridges blocks import of authentic precursors into mitochondria and allows quantitation of import sites
    • Vestweber D., and Schatz G. A chimeric mitochondrial precursor protein with internal disulfide bridges blocks import of authentic precursors into mitochondria and allows quantitation of import sites. J. Cell Biol. 107 (1988) 2037-2043
    • (1988) J. Cell Biol. , vol.107 , pp. 2037-2043
    • Vestweber, D.1    Schatz, G.2
  • 78
    • 0029583409 scopus 로고
    • The mitochondrial protein import machinery: Role of ATP in dissociation of the Hsp70. Mim44 complex
    • Von Ahsen O., Voos W., Henninger H., and Pfanner N. The mitochondrial protein import machinery: Role of ATP in dissociation of the Hsp70. Mim44 complex. J. Biol. Chem. 270 (1995) 29848-29853
    • (1995) J. Biol. Chem. , vol.270 , pp. 29848-29853
    • Von Ahsen, O.1    Voos, W.2    Henninger, H.3    Pfanner, N.4
  • 79
    • 0027362778 scopus 로고
    • Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix
    • Voos W., Gambill D., Guiard B., Pfanner N., and Craig E.A. Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix. J. Cell Biol. 123 (1993) 119-126
    • (1993) J. Cell Biol. , vol.123 , pp. 119-126
    • Voos, W.1    Gambill, D.2    Guiard, B.3    Pfanner, N.4    Craig, E.A.5
  • 80
    • 0027994692 scopus 로고
    • Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across the membranes
    • Voos W., Gambill B.D., Laloraya S., Ang D., Craig E.A., and Pfanner N. Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across the membranes. Mol. Cell. Biol. 14 (1994) 6627-6634
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6627-6634
    • Voos, W.1    Gambill, B.D.2    Laloraya, S.3    Ang, D.4    Craig, E.A.5    Pfanner, N.6
  • 81
    • 0029934520 scopus 로고    scopus 로고
    • Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins
    • Voos W., von Ahsen O., Müller H., Guiard B., Rassow J., and Pfanner N. Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins. EMBO J. 15 (1996) 2668-2677
    • (1996) EMBO J. , vol.15 , pp. 2668-2677
    • Voos, W.1    von Ahsen, O.2    Müller, H.3    Guiard, B.4    Rassow, J.5    Pfanner, N.6
  • 83
    • 0024008659 scopus 로고
    • MASI, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease
    • Witte C., Jensen R.E., Yaffe M.P., and Schatz G. MASI, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease. EMBO J. 7 (1988) 1439-1447
    • (1988) EMBO J. , vol.7 , pp. 1439-1447
    • Witte, C.1    Jensen, R.E.2    Yaffe, M.P.3    Schatz, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.